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Literature summary extracted from

  • Contestabile, R.; Paiardini, A.; Pascarella, S.; Di Salvo, M.L.; D'Aguanno, S.; Bossa, F.
    L-Threonine aldolase, serine hydroxymethyltransferase and fungal alanine racemase. A subgroup of strictly related enzymes specialized for different functions (2001), Eur. J. Biochem., 268, 6508-6525.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.2.1
-
Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.2.1 D-alanine inactivates enzyme by converting the enzyme bound pyridoxal 5'-phosphate to pyridoxamine phosphate in a transamination reaction Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.1.2.1 Escherichia coli P0A825
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine mechanism Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.2.1 L-serine + tetrahydrofolate
-
Escherichia coli glycine + 5,10-methylenetetrahydrofolate + H2O
-
r
2.1.2.1 additional information enzyme catalyzes the pyridoxal 5'-phosphate dependent reversible cleavage of 3-hydroxy-alpha-amino acids Escherichia coli ?
-
?
2.1.2.1 additional information enzyme transaminates D-alanine to pyruvate and pyridoxamine phosphate Escherichia coli ?
-
?
2.1.2.1 additional information enzyme catalyses the racemization of D- and L-alanine Escherichia coli ?
-
?